3j6e: Difference between revisions
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==Energy minimized average structure of Microtubules stabilized by GmpCpp== | ==Energy minimized average structure of Microtubules stabilized by GmpCpp== | ||
<StructureSection load='3j6e' size='340' side='right' caption='[[3j6e]], [[Resolution|resolution]] 4.70Å' scene=''> | <StructureSection load='3j6e' size='340' side='right' caption='[[3j6e]], [[Resolution|resolution]] 4.70Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=G2P:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>G2P</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=G2P:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>G2P</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3j6f|3j6f]], [[3j6g|3j6g]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3j6f|3j6f]], [[3j6g|3j6g]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j6e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j6e RCSB], [http://www.ebi.ac.uk/pdbsum/3j6e PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j6e OCA], [http://pdbe.org/3j6e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j6e RCSB], [http://www.ebi.ac.uk/pdbsum/3j6e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j6e ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3j6e" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Tubulin|Tubulin]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 01:33, 5 August 2016
Energy minimized average structure of Microtubules stabilized by GmpCppEnergy minimized average structure of Microtubules stabilized by GmpCpp
Structural highlights
Function[TBA1A_PIG] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. [TBB_PIG] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. Publication Abstract from PubMedDynamic instability, the stochastic switching between growth and shrinkage, is essential for microtubule function. This behavior is driven by GTP hydrolysis in the microtubule lattice and is inhibited by anticancer agents like Taxol. We provide insight into the mechanism of dynamic instability, based on high-resolution cryo-EM structures (4.7-5.6 A) of dynamic microtubules and microtubules stabilized by GMPCPP or Taxol. We infer that hydrolysis leads to a compaction around the E-site nucleotide at longitudinal interfaces, as well as movement of the alpha-tubulin intermediate domain and H7 helix. Displacement of the C-terminal helices in both alpha- and beta-tubulin subunits suggests an effect on interactions with binding partners that contact this region. Taxol inhibits most of these conformational changes, allosterically inducing a GMPCPP-like state. Lateral interactions are similar in all conditions we examined, suggesting that microtubule lattice stability is primarily modulated at longitudinal interfaces. High-Resolution Microtubule Structures Reveal the Structural Transitions in alphabeta-Tubulin upon GTP Hydrolysis.,Alushin GM, Lander GC, Kellogg EH, Zhang R, Baker D, Nogales E Cell. 2014 May 22;157(5):1117-29. doi: 10.1016/j.cell.2014.03.053. PMID:24855948[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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